3hsf
From Proteopedia
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| - | + | {{STRUCTURE_3hsf| PDB=3hsf | SCENE= }} | |
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'''HEAT SHOCK TRANSCRIPTION FACTOR (HSF)''' | '''HEAT SHOCK TRANSCRIPTION FACTOR (HSF)''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | 3HSF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Kluyveromyces_lactis Kluyveromyces lactis]. This structure supersedes the now removed PDB entry | + | 3HSF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Kluyveromyces_lactis Kluyveromyces lactis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2hsf 2hsf]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HSF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Pelton, J G.]] | [[Category: Pelton, J G.]] | ||
[[Category: Wemmer, D E.]] | [[Category: Wemmer, D E.]] | ||
| - | [[Category: | + | [[Category: Transcription regulation]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:04:12 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 19:04, 4 May 2008
HEAT SHOCK TRANSCRIPTION FACTOR (HSF)
Overview
The solution structure of the 92 residue (11 kDa) winged helix-turn-helix DNA-binding domain from the kluyveromyces lactis heat shock factor was refined using a total of 932 NOE, 35 phi, 25 chi 1, 5 chi 2 and 44 hydrogen bond restraints. The overall root-mean-square deviation for structured regions was 0.75(+/- 0.15) A. The three-helix bundle and four-stranded beta-sheet are well defined with rmsd of 0.53(+/- 0.10) A and 0.60(+/- 0.17) A, respectively. Helix H2 is underwound and bent near Pro45. The angle between helix H2 and the proposed recognition helix H3 is 96(+/- 6) degrees. Detailed comparisons are made with the X-ray structure of this protein as well as other structural studies on HSF. Overall, the results are consistent with the earlier studies. Differences are related to protein-protein interactions in the crystal and dynamics in solution. Backbone dynamics was investigated via 15N relaxation. The average R1, R2 and NOE values for residues in segments of secondary structure were 1.9(+/- 0.9) s-1, 7.8(+/- 0.9) s-1 and 0.81(+/- 0.05), respectively. The correlation time based on these data was 5.6(+/- 0.4) ns. Motional order parameters were calculated by fitting the relaxation data to one of three models. Low-order parameters were found for residues that comprise the turn between helices H2 and H3 (residues Lys49 to Phe53), and most strikingly, the 16 residue wing (residues Val68 to Arg83). These data are consistent with the lack of long-range NOEs identified in these regions. The data provide a basis for comparison with results of the protein-DNA complex. The relationship between structure and function is discussed.
About this Structure
3HSF is a Single protein structure of sequence from Kluyveromyces lactis. This structure supersedes the now removed PDB entry 2hsf. Full crystallographic information is available from OCA.
Reference
Refined solution structure and dynamics of the DNA-binding domain of the heat shock factor from Kluyveromyces lactis., Damberger FF, Pelton JG, Liu C, Cho H, Harrison CJ, Nelson HC, Wemmer DE, J Mol Biol. 1995 Dec 8;254(4):704-19. PMID:7500344 Page seeded by OCA on Sun May 4 22:04:12 2008
